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NADH dehydrogenase |
Identifiers |
EC number |
1.6.99.3 |
CAS number |
9079-67-8 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
|
NADH dehydrogenase (EC 1.6.99.3, cytochrome c reductase, type 1 dehydrogenase, beta-NADH dehydrogenase dinucleotide, diaphorase, dihydrocodehydrogenase I dehydrogenase, dihydronicotinamide adenine dinucleotide dehydrogenase, diphosphopyridine diaphorase, DPNH diaphorase, NADH diaphorase, NADH hydrogenase, NADH oxidoreductase, NADH-menadione oxidoreductase, reduced diphosphopyridine nucleotide diaphorase) is an enzyme with systematic name NADH:acceptor oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction
- NADH + H+ + acceptor NAD+ + reduced acceptor
NADH dehydrogenase is a flavoprotein that contains iron-sulfur centres.
References
- ^ Adachi, K. and Okuyama, T. (1972). "Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes". Biochim. Biophys. Acta 268: 629–637. doi:10.1016/0005-2744(72)90266-5. PMID 4402556.
- ^ Hatefi, Y., Ragan, C.I. and Galante, Y.M. (1985). "The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system". In Martonosi, A. The Enzymes of Biological Membranes 4 (2nd ed.). New York: Plenum Press. pp. 1–70.
- ^ Hochstein, L.I. and Dalton, B.P. (1973). "Studies of a halophilic NADH dehydrogenase. I. Purification and properties of the enzyme". Biochim. Biophys. Acta 302: 216–228. doi:10.1016/0005-2744(73)90150-2. PMID 4144655.
- ^ Kaniuga, Z. (1963). "The transformation of mitochondrial NADH dehydrogenase into NADH:Cytochrome c oxidoreductase". Biochim. Biophys. Acta 73: 550–564. doi:10.1016/0926-6569(63)90175-5. PMID 14074130.
See also
- NADH dehydrogenase (ubiquinone)
- NADH dehydrogenase (quinone)
External links
- NADH dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
UpToDate Contents
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Japanese Journal
- 〈Original Papers〉Highly rearranged mitochondrial genome of the bivalve pearl oyster Pinctada fucata
- Okumura Nao,Oishi Mei,Okayama Kazuki,Miyamoto Hiroshi
- Memoirs of the Faculty of Biology-Oriented Science and Technology of Kinki University (29), 1-6, 2012-3
- … The deduced amino acid sequences of one fragment corresponded to cytochrome b and NADH dehydrogenase subunit 2. … The other fragment contained regions corresponding to ATP synthase subunit 6, cytochrome c oxidase subunit III, and NADH dehydrogenase subunit 3. …
- NAID 120004009246
- Mitochondrial dysfunction, a probable cause of persistent oxidative stress after exposure to ionizing radiation
- Yoshida Takako,Goto Shinji,Kawakatsu Miho,Urata Yoshishige,Li Tao-sheng
- Free Radical Research 46(2), 147-153, 2012-02
- … First, a robust increase of intracellular ROS levels occurred within minutes, but the intracellular ROS disappeared within 30 min. Then the mitochondrial dysfunction was detected at 12 h after irradiation, as indicated by the decreased activity of NADH dehydrogenase (Complex I), the most important enzyme in regulating the release of ROS from the mitochondrial electron transport chain (ETC). …
- NAID 120003874183
Related Links
- NADH de·hy·dro·gen·ase. an iron-sulfur-containing flavoprotein reversibly oxidizing NADH to NAD +; an inherited deficiency of this complex results in overwhelming ...
- So what exactly is NADH? It is a naturally‐occurring and vital compound found in all living cells of plants, animals, and humans. It is essential for adequate ...
Related Pictures
★リンクテーブル★
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- 英
- NADH dehydrogenase
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- NADHデヒドロゲナーゼ
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- 英
- NADH dehydrogenase
- 関
- NADH脱水素酵素
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還元型ニコチンアミドアデニンジヌクレオチド reduced nicotinamideadenine dinucleotide reduced NAD
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脱水素酵素 デヒドロゲナーゼ
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脱水素酵素 デヒドロゲナーゼ